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Conserved domains on  [gi|219842214|ref|NP_001137358|]
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protein phosphatase 1 regulatory subunit 12A isoform b [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 844-943 1.83e-43

cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of protein phosphatase 1 regulatory subunits 12A, 12B and 12C. In protein phosphatase 1 regulatory subunit 12A it has been found to bind to cGMP-dependent protein kinase 1 via a leucine zipper motif located at the C-terminus of this domain.


:

Pssm-ID: 464927 [Multi-domain]  Cd Length: 102  Bit Score: 152.84  E-value: 1.83e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214  844 DFKKLYEQILAENEKLKAQLHDTNMELTDLKLQLEKAT-QRQERFADRS-LLEMEKRERRALERRISEMEEELKMLPDLK 921
Cdd:pfam15898   1 DYKKLYEEELQENERLKRKLQDAQQELAELKSQLERLTqQRQESFSDRSsLLETEKREKRALERKISEMEEELKVLEDLR 80

                          90       100
                  ....*....|....*....|..
gi 219842214  922 ADNQRLKDENGALIRVISKLSK 943
Cdd:pfam15898  81 AENQRLKDENGALIRVISKLSK 102
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-244 2.20e-34

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.54  E-value: 2.20e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214   1 MVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLdiaeeeameellqnevnrqgvdIE 80
Cdd:COG0666   69 VALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPL----------------------HL 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214  81 AARKEEERImlrdARQWLNSG-HINdvRHAKSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEE 159
Cdd:COG0666  127 AAYNGNLEI----VKLLLEAGaDVN--AQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLE 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214 160 ACRILVDNLCDMEMVNKVGQTAFDVADEDILGYLEELQKKQNLLHSEKRDKKSPLIESTANMDNNQSQKTFKNKETLIIE 239
Cdd:COG0666  201 IVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280


                 ....*
gi 219842214 240 PEKNA 244
Cdd:COG0666  281 ALLDL 285
IPD_MYPT1 cd21944
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1(MYPT1); MYPT1, ...
 571-627 8.20e-19

inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1(MYPT1); MYPT1, also called protein phosphatase 1 regulatory subunit 12A (PPP1R12A), myosin phosphatase target subunit 1, or protein phosphatase myosin-binding subunit, is the targeting subunit of smooth-muscle myosin phosphatase. It is a substrate for the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH). MYPT1 acts as a key regulator of protein phosphatase 1C (PPP1C). It mediates binding to myosin. As part of the PPP1C complex, MYPT1 is involved in dephosphorylation of the mitosis regulator polo-like kinase 1 (PLK1). It is capable of inhibiting HIF1A inhibitor (HIF1AN)-dependent suppression of HIF1A activity. This model corresponds to the inhibitory phosphorylation domain of MYPT1.


:

Pssm-ID: 412019  Cd Length: 57  Bit Score: 81.11  E-value: 8.20e-19
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 219842214 571 STTEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRS 627
Cdd:cd21944    1 STSEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRS 57
 
Name Accession Description Interval E-value
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 844-943 1.83e-43

cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of protein phosphatase 1 regulatory subunits 12A, 12B and 12C. In protein phosphatase 1 regulatory subunit 12A it has been found to bind to cGMP-dependent protein kinase 1 via a leucine zipper motif located at the C-terminus of this domain.


Pssm-ID: 464927 [Multi-domain]  Cd Length: 102  Bit Score: 152.84  E-value: 1.83e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214  844 DFKKLYEQILAENEKLKAQLHDTNMELTDLKLQLEKAT-QRQERFADRS-LLEMEKRERRALERRISEMEEELKMLPDLK 921
Cdd:pfam15898   1 DYKKLYEEELQENERLKRKLQDAQQELAELKSQLERLTqQRQESFSDRSsLLETEKREKRALERKISEMEEELKVLEDLR 80

                          90       100
                  ....*....|....*....|..
gi 219842214  922 ADNQRLKDENGALIRVISKLSK 943
Cdd:pfam15898  81 AENQRLKDENGALIRVISKLSK 102
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-244 2.20e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.54  E-value: 2.20e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214   1 MVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLdiaeeeameellqnevnrqgvdIE 80
Cdd:COG0666   69 VALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPL----------------------HL 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214  81 AARKEEERImlrdARQWLNSG-HINdvRHAKSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEE 159
Cdd:COG0666  127 AAYNGNLEI----VKLLLEAGaDVN--AQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLE 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214 160 ACRILVDNLCDMEMVNKVGQTAFDVADEDILGYLEELQKKQNLLHSEKRDKKSPLIESTANMDNNQSQKTFKNKETLIIE 239
Cdd:COG0666  201 IVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280


                 ....*
gi 219842214 240 PEKNA 244
Cdd:COG0666  281 ALLDL 285
IPD_MYPT1 cd21944
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1(MYPT1); MYPT1, ...
 571-627 8.20e-19

inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1(MYPT1); MYPT1, also called protein phosphatase 1 regulatory subunit 12A (PPP1R12A), myosin phosphatase target subunit 1, or protein phosphatase myosin-binding subunit, is the targeting subunit of smooth-muscle myosin phosphatase. It is a substrate for the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH). MYPT1 acts as a key regulator of protein phosphatase 1C (PPP1C). It mediates binding to myosin. As part of the PPP1C complex, MYPT1 is involved in dephosphorylation of the mitosis regulator polo-like kinase 1 (PLK1). It is capable of inhibiting HIF1A inhibitor (HIF1AN)-dependent suppression of HIF1A activity. This model corresponds to the inhibitory phosphorylation domain of MYPT1.


Pssm-ID: 412019  Cd Length: 57  Bit Score: 81.11  E-value: 8.20e-19
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 219842214 571 STTEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRS 627
Cdd:cd21944    1 STSEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRS 57
Ank_2 pfam12796
Ankyrin repeats (3 copies);
116-185 6.77e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.61  E-value: 6.77e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214  116 LHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNlCDMEMVNKvGQTAFDVA 185
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYA 68
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1-185 1.07e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 74.68  E-value: 1.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214   1 MVKFLVENGANINQPDNEGWIPLHAaascgYL-------DIAEFLIGQGAHVGAVNSEGDTPLDIAeeeameellqneVN 73
Cdd:PHA03095  99 VIKLLIKAGADVNAKDKVGRTPLHV-----YLsgfninpKVIRLLLRKGADVNALDLYGMTPLAVL------------LK 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214  74 RQGVDIEAARkeeeriMLRDArqwlnsghINDVRHAKS-GGTALHVAA--AKGYTEVLKLLIQAGYDVNIKDYDGWTPLH 150
Cdd:PHA03095 162 SRNANVELLR------LLIDA--------GADVYAVDDrFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLH 227

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 219842214 151 AAAHWGkeeACR-ILVDNL----CDMEMVNKVGQTAFDVA 185
Cdd:PHA03095 228 SMATGS---SCKrSLVLPLliagISINARNRYGQTPLHYA 264
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 114-140 1.08e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.88  E-value: 1.08e-04
                           10        20
                   ....*....|....*....|....*..
gi 219842214   114 TALHVAAAKGYTEVLKLLIQAGYDVNI 140
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 780-943 2.53e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 2.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214 780 QEQQSDTEEGSNKKETQTDSISRYETSSTSAGDRYDSLLGRSGSYSYLEERKPY-SSRLEKDDSTDFKK---LYEQILAE 855
Cdd:COG4942   68 ARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPlALLLSPEDFLDAVRrlqYLKYLAPA 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214 856 NEKLKAQLHDTNMELTDLKLQLEKATQRQERF-----ADRSLLEMEKRERRALERRI-SEMEEELKMLPDLKADNQRLKD 929
Cdd:COG4942  148 RREQAEELRADLAELAALRAELEAERAELEALlaeleEERAALEALKAERQKLLARLeKELAELAAELAELQQEAEELEA 227

                        170
                 ....*....|....
gi 219842214 930 ENGALIRVISKLSK 943
Cdd:COG4942  228 LIARLEAEAAAAAE 241
 
Name Accession Description Interval E-value
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
 844-943 1.83e-43

cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of protein phosphatase 1 regulatory subunits 12A, 12B and 12C. In protein phosphatase 1 regulatory subunit 12A it has been found to bind to cGMP-dependent protein kinase 1 via a leucine zipper motif located at the C-terminus of this domain.


Pssm-ID: 464927 [Multi-domain]  Cd Length: 102  Bit Score: 152.84  E-value: 1.83e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214  844 DFKKLYEQILAENEKLKAQLHDTNMELTDLKLQLEKAT-QRQERFADRS-LLEMEKRERRALERRISEMEEELKMLPDLK 921
Cdd:pfam15898   1 DYKKLYEEELQENERLKRKLQDAQQELAELKSQLERLTqQRQESFSDRSsLLETEKREKRALERKISEMEEELKVLEDLR 80

                          90       100
                  ....*....|....*....|..
gi 219842214  922 ADNQRLKDENGALIRVISKLSK 943
Cdd:pfam15898  81 AENQRLKDENGALIRVISKLSK 102
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-244 2.20e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.54  E-value: 2.20e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214   1 MVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLdiaeeeameellqnevnrqgvdIE 80
Cdd:COG0666   69 VALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPL----------------------HL 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214  81 AARKEEERImlrdARQWLNSG-HINdvRHAKSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEE 159
Cdd:COG0666  127 AAYNGNLEI----VKLLLEAGaDVN--AQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLE 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214 160 ACRILVDNLCDMEMVNKVGQTAFDVADEDILGYLEELQKKQNLLHSEKRDKKSPLIESTANMDNNQSQKTFKNKETLIIE 239
Cdd:COG0666  201 IVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280


                 ....*
gi 219842214 240 PEKNA 244
Cdd:COG0666  281 ALLDL 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-182 1.98e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 107.35  E-value: 1.98e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214   1 MVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLdiaeeeameellqnevnrqgvdIE 80
Cdd:COG0666  135 IVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL----------------------HL 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214  81 AARKEEERIMlrdarQWLNSGHINDVRHAKSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEA 160
Cdd:COG0666  193 AAENGHLEIV-----KLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALI 267

                        170       180
                 ....*....|....*....|..
gi 219842214 161 CRILVDNLCDMEMVNKVGQTAF 182
Cdd:COG0666  268 VKLLLLALLLLAAALLDLLTLL 289
IPD_MYPT1 cd21944
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1(MYPT1); MYPT1, ...
 571-627 8.20e-19

inhibitory phosphorylation domain of myosin phosphatase targeting subunit 1(MYPT1); MYPT1, also called protein phosphatase 1 regulatory subunit 12A (PPP1R12A), myosin phosphatase target subunit 1, or protein phosphatase myosin-binding subunit, is the targeting subunit of smooth-muscle myosin phosphatase. It is a substrate for the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH). MYPT1 acts as a key regulator of protein phosphatase 1C (PPP1C). It mediates binding to myosin. As part of the PPP1C complex, MYPT1 is involved in dephosphorylation of the mitosis regulator polo-like kinase 1 (PLK1). It is capable of inhibiting HIF1A inhibitor (HIF1AN)-dependent suppression of HIF1A activity. This model corresponds to the inhibitory phosphorylation domain of MYPT1.


Pssm-ID: 412019  Cd Length: 57  Bit Score: 81.11  E-value: 8.20e-19
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 219842214 571 STTEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRS 627
Cdd:cd21944    1 STSEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRS 57
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
78-193 1.18e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 84.62  E-value: 1.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214  78 DIEAARKEEERIMLRDARQWLNSGHINDVRHAKSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGK 157
Cdd:COG0666   53 LGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGN 132

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 219842214 158 EEACRILVDNLCDMEMVNKVGQTAFDVA----DEDILGYL 193
Cdd:COG0666  133 LEIVKLLLEAGADVNAQDNDGNTPLHLAaangNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
116-185 6.77e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.61  E-value: 6.77e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214  116 LHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNlCDMEMVNKvGQTAFDVA 185
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYA 68
IPD_PPP1R12C cd21945
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12C (PPP1R12C); ...
 573-626 5.95e-15

inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12C (PPP1R12C); PPP1R12C, also called protein phosphatase 1 myosin-binding subunit of 85 kDa (MBS85), protein phosphatase 1 myosin-binding subunit p85, or LENG3, regulates myosin phosphatase activity. This model corresponds to a conserved region of PPP1R12C, which shows high sequence similarity to the inhibitory phosphorylation domain of MYPT1.


Pssm-ID: 412020  Cd Length: 54  Bit Score: 69.73  E-value: 5.95e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 219842214 573 TEVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGR 626
Cdd:cd21945    1 TDSRDRRRSYQTPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKSIGK 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1-185 1.07e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 74.68  E-value: 1.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214   1 MVKFLVENGANINQPDNEGWIPLHAaascgYL-------DIAEFLIGQGAHVGAVNSEGDTPLDIAeeeameellqneVN 73
Cdd:PHA03095  99 VIKLLIKAGADVNAKDKVGRTPLHV-----YLsgfninpKVIRLLLRKGADVNALDLYGMTPLAVL------------LK 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214  74 RQGVDIEAARkeeeriMLRDArqwlnsghINDVRHAKS-GGTALHVAA--AKGYTEVLKLLIQAGYDVNIKDYDGWTPLH 150
Cdd:PHA03095 162 SRNANVELLR------LLIDA--------GADVYAVDDrFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLH 227

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 219842214 151 AAAHWGkeeACR-ILVDNL----CDMEMVNKVGQTAFDVA 185
Cdd:PHA03095 228 SMATGS---SCKrSLVLPLliagISINARNRYGQTPLHYA 264
Ank_2 pfam12796
Ankyrin repeats (3 copies);
1-142 1.09e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.45  E-value: 1.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214    1 MVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQgahvgavnsegdtpldiaeeeameellqnevnrqgvdie 80
Cdd:pfam12796  12 LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH--------------------------------------- 52

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 219842214   81 aarkeeerimlrdarqwlnsghiNDVRHAKSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKD 142
Cdd:pfam12796  53 -----------------------ADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
94-175 5.20e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 5.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214   94 ARQWLNSGHINDVRHaKSGGTALHVAAAKGYTEVLKLLIQAGyDVNIKDYdGWTPLHAAAHWGKEEACRILVDNLCDMEM 173
Cdd:pfam12796  13 VKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIVKLLLEKGADINV 89


                  ..
gi 219842214  174 VN 175
Cdd:pfam12796  90 KD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
112-165 7.68e-13

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 63.83  E-value: 7.68e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 219842214  112 GGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILV 165
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 2-153 9.02e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 71.23  E-value: 9.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214   2 VKFLVENGANINQPDNEGWIPLHAAASC--GYLDIAEFLIGQGAHVGAVNSEGDTPLDIAEEEAMEELL--QNEVNRqGV 77
Cdd:PHA03100  89 VKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKilKLLIDK-GV 167

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 219842214  78 DIEAARKEEeriMLrdarqwLNSG-HIN--DVRhaksGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAA 153
Cdd:PHA03100 168 DINAKNRVN---YL------LSYGvPINikDVY----GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI 233
IPD_MYPT2 cd21946
inhibitory phosphorylation domain of myosin phosphatase targeting subunit 2 (MYPT2); MYPT2, ...
 576-628 2.57e-11

inhibitory phosphorylation domain of myosin phosphatase targeting subunit 2 (MYPT2); MYPT2, also called protein phosphatase 1 regulatory subunit 12B (PPP1R12B), or myosin phosphatase target subunit 2, is the targeting subunit of smooth-muscle myosin phosphatase that regulates myosin phosphatase activity and augments Ca(2+) sensitivity of the contractile apparatus. This model corresponds to the inhibitory phosphorylation domain of MYPT2.


Pssm-ID: 412021  Cd Length: 53  Bit Score: 59.67  E-value: 2.57e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 219842214 576 RERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKTIGRSR 628
Cdd:cd21946    1 REKRRSYLTPVRDEEAESLRKARSRQARQTRRSTQGVTLTDLQEAERTFSRSR 53
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1-176 9.00e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.20  E-value: 9.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214   1 MVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDIAEEEAMEELLQNEVNRQGVDIe 80
Cdd:PHA02878 183 LTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDV- 261

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214  81 aarkeeerimlrdarqwlnsghindvrHAKS---GGTALHVAAAKgyTEVLKLLIQAGYDVNIKDYDGWTPLHAAA-HWG 156
Cdd:PHA02878 262 ---------------------------NAKSyilGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVkQYL 312

                        170       180
                 ....*....|....*....|
gi 219842214 157 KEEACRILVDNLCDMEMVNK 176
Cdd:PHA02878 313 CINIGRILISNICLLKRIKP 332
IPD_PPP1R12 cd21930
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12 (PPP1R12) ...
 576-622 9.42e-10

inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12 (PPP1R12) family; The PPP1R12 family includes PPP1R12A/MYPT1, PPP1R12B/MYPT2, and PPP1R12C. PPP1R12A/MYPT1, also called myosin phosphatase target subunit 1, or protein phosphatase myosin-binding subunit, is a substrate for the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH). It acts as a key regulator of protein phosphatase 1C (PPP1C). It mediates binding to myosin. As part of the PPP1C complex, PPP1R12A/MYPT1 is involved in dephosphorylation of PLK1. It is capable of inhibiting HIF1A inhibitor (HIF1AN)-dependent suppression of HIF1A activity. PPP1R12B/MYPT2, also called myosin phosphatase target subunit 2, is the targeting subunit of smooth-muscle myosin phosphatase that regulates myosin phosphatase activity and augments Ca(2+) sensitivity of the contractile apparatus. PPP1R12C, also called protein phosphatase 1 myosin-binding subunit of 85 kDa (MBS85), protein phosphatase 1 myosin-binding subunit p85, or LENG3, regulates myosin phosphatase activity. All family members contain an inhibitory phosphorylation domain.


Pssm-ID: 412018  Cd Length: 47  Bit Score: 54.66  E-value: 9.42e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 219842214 576 RERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEK 622
Cdd:cd21930    1 RSRRRSYLPPVRDEESETQRKARAKRARQTRRSTQGVTLEDLEEAEK 47
IPD_PPP1R12A-like cd22527
inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12A-like, and ...
 574-623 9.44e-10

inhibitory phosphorylation domain of protein phosphatase 1 regulatory subunit 12A-like, and similar proteins; Protein phosphatase 1 regulatory subunit 12A-like (PPP1R12A-like) is a homolog of MYPT1, also called protein phosphatase 1 regulatory subunit 12A (PPP1R12A), myosin phosphatase target subunit 1, or protein phosphatase myosin-binding subunit. MYPT1 is the targeting subunit of smooth-muscle myosin phosphatase. It is a substrate for the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH). MYPT1 acts as a key regulator of protein phosphatase 1C (PPP1C). It mediates binding to myosin. As part of the PPP1C complex, MYPT1 is involved in dephosphorylation of the mitosis regulator polo-like kinase 1 (PLK1). It is capable of inhibiting HIF1A inhibitor (HIF1AN)-dependent suppression of HIF1A activity. This model corresponds to the inhibitory phosphorylation domain of PPP1R12A-like protein.


Pssm-ID: 412022  Cd Length: 50  Bit Score: 54.88  E-value: 9.44e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 219842214 574 EVRERRRSYLTPVRDEESESQRKARSRQARQSRRSTQGVTLTDLQEAEKT 623
Cdd:cd22527    1 ETKERRRSYLTPVRDEEAEAQRKARSRHARQSRRSTQGVTLTDLKEAEKT 50
PHA03095 PHA03095
ankyrin-like protein; Provisional
 1-149 1.98e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 61.19  E-value: 1.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214   1 MVKFLVENGANINQPDNEGWIPLHA-----AAScgyLDIAEFLIGQGAHVGAVNSEGDTPLDIAEEEAMEELLQN-EVNR 74
Cdd:PHA03095 134 VIRLLLRKGADVNALDLYGMTPLAVllksrNAN---VELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARIVrELIR 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214  75 QGVDiEAARKEEERIMLRDA-----------RQWLNSGHINDVRHaKSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDY 143
Cdd:PHA03095 211 AGCD-PAATDMLGNTPLHSMatgssckrslvLPLLIAGISINARN-RYGQTPLHYAAVFNNPRACRRLIALGADINAVSS 288


                 ....*.
gi 219842214 144 DGWTPL 149
Cdd:PHA03095 289 DGNTPL 294
Ank_5 pfam13857
Ankyrin repeats (many copies);
5-58 2.81e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.89  E-value: 2.81e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 219842214    5 LVENG-ANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDI 58
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1-192 3.06e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 60.28  E-value: 3.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214   1 MVKFLVENGANINQPD-NEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDiaeeeameellqnevnrqgvdi 79
Cdd:PHA02878 149 ITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLH---------------------- 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214  80 EAARKEEERIMlrdaRQWLNSGHINDVRHaKSGGTALHVAAA--KGYtEVLKLLIQAGYDVNIKDY-DGWTPLHAAAHwg 156
Cdd:PHA02878 207 HAVKHYNKPIV----HILLENGASTDARD-KCGNTPLHISVGycKDY-DILKLLLEHGVDVNAKSYiLGLTALHSSIK-- 278

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 219842214 157 KEEACRILVDNLCDMEMVNKVGQTAFDVADEDILGY 192
Cdd:PHA02878 279 SERKLKLLLEYGADINSLNSYKLTPLSSAVKQYLCI 314
Ank_4 pfam13637
Ankyrin repeats (many copies);
1-39 8.56e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 8.56e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 219842214    1 MVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLI 39
Cdd:pfam13637  16 LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 1-180 9.23e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.52  E-value: 9.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214   1 MVKFLVENGANINQPDNEGWIPLHAAASCGY-----LDIAEFLIGQGAHVGAVNSEGDTPLDIAeeeameellqnevnrq 75
Cdd:PHA03100  50 VVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYA---------------- 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214  76 gvdieAARKEEERIMLRDarqwLNSGHINDVRHAKSGGTALHVAAAKGY--TEVLKLLIQAGYDVNIKD-------YD-- 144
Cdd:PHA03100 114 -----ISKKSNSYSIVEY----LLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNrvnyllsYGvp 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 219842214 145 -------GWTPLHAAAHWGKEEACRILVDNLCDMEMVNKVGQT 180
Cdd:PHA03100 185 inikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDT 227
PHA03095 PHA03095
ankyrin-like protein; Provisional
 2-205 1.10e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.42  E-value: 1.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214   2 VKFLVENGANINQPDNEGWIPLHAAASCG---YLDIAEFLIGQGAHVGAVNSEGDTPLDIaeeeamEELLQNEVN----- 73
Cdd:PHA03095  30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPLHL------YLYNATTLDvikll 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214  74 -RQGVDIEAarkeeerimlRDarqwlnsghindvrhaKSGGTALHVAAAKGYT--EVLKLLIQAGYDVNIKDYDGWTPLH 150
Cdd:PHA03095 104 iKAGADVNA----------KD----------------KVGRTPLHVYLSGFNInpKVIRLLLRKGADVNALDLYGMTPLA 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 219842214 151 AaahwgkeeacrILVDNLCDMEMVNKVGQTAFDVADEDILGyleelqkkQNLLHS 205
Cdd:PHA03095 158 V-----------LLKSRNANVELLRLLIDAGADVYAVDDRF--------RSLLHH 193
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
70-193 1.31e-07

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 54.19  E-value: 1.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214  70 NEVNRQGVDIEAARKEEERIMLRDARQWLNSGHINDVRHAKSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPL 149
Cdd:COG0666   12 LAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLL 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 219842214 150 HAAAHWGKEEACRILVDNLCDMEMVNKVGQTAFDVA----DEDILGYL 193
Cdd:COG0666   92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAayngNLEIVKLL 139
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1-167 1.35e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.97  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214   1 MVKFLVENGAN-INQPDNEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPL----DIAEEEAMEELLQNEVNRQ 75
Cdd:PHA02874  16 AIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLltaiKIGAHDIIKLLIDNGVDTS 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214  76 GVDIEAARKEEERIMlrdarqwLNSGHINDVRHAKSgGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHW 155
Cdd:PHA02874  96 ILPIPCIEKDMIKTI-------LDCGIDVNIKDAEL-KTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKH 167

                        170
                 ....*....|..
gi 219842214 156 GKEEACRILVDN 167
Cdd:PHA02874 168 NFFDIIKLLLEK 179
Ank_5 pfam13857
Ankyrin repeats (many copies);
98-152 1.77e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 1.77e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 219842214   98 LNSGHINDVRHAKSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAA 152
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 120-206 5.14e-07

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.75  E-value: 5.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214 120 AAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMEMVNKVGQTAFDVADEDILGYLEELQKK 199
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169


                 ....*..
gi 219842214 200 QNLLHSE 206
Cdd:PTZ00322 170 HSQCHFE 176
Ank_4 pfam13637
Ankyrin repeats (many copies);
145-193 2.40e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 2.40e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 219842214  145 GWTPLHAAAHWGKEEACRILVDNLCDMEMVNKVGQTAFDVA----DEDILGYL 193
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAasngNVEVLKLL 53
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1-167 3.98e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 50.35  E-value: 3.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214   1 MVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAHVG----------AVNSEGDTPLDIAEEEAMEELLQN 70
Cdd:PHA02874  50 IVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSilpipciekdMIKTILDCGIDVNIKDAELKTFLH 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214  71 EVNRQGvDIEAARkeeeriMLRDARQWLNSGHINdvrhaksGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLH 150
Cdd:PHA02874 130 YAIKKG-DLESIK------MLFEYGADVNIEDDN-------GCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195

                        170
                 ....*....|....*..
gi 219842214 151 AAAHWGKEEACRILVDN 167
Cdd:PHA02874 196 NAAEYGDYACIKLLIDH 212
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 112-142 5.53e-06

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.82  E-value: 5.53e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 219842214  112 GGTALHVAAAK-GYTEVLKLLIQAGYDVNIKD 142
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1-192 8.47e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 49.68  E-value: 8.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214   1 MVKFLVENGANINQPDNEGWIPLHAAASCGY-LDIAEFLIGQGAHVGAVNSEGDTPLDIAEEEAMEELLQNEVNRQGVDI 79
Cdd:PHA02876 289 LVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITLLELGANV 368

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214  80 EAaRKEEERIMLRDARQWLNSGHINDVRH--------AKSGGTALHVA--AAKGYTEVlKLLIQAGYDVNIKDYDGWTPL 149
Cdd:PHA02876 369 NA-RDYCDKTPIHYAAVRNNVVIINTLLDygadiealSQKIGTALHFAlcGTNPYMSV-KTLIDRGANVNSKNKDLSTPL 446

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 219842214 150 HAAAHWG-KEEACRILVDNLCDMEMVNKVGQTAFDVAdediLGY 192
Cdd:PHA02876 447 HYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA----LEY 486
Ank_5 pfam13857
Ankyrin repeats (many copies);
131-185 1.55e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 1.55e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 219842214  131 LIQAGY-DVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMEMVNKVGQTAFDVA 185
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1-200 1.65e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.42  E-value: 1.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214   1 MVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLdiaeeeameellQNEV--NRQGVD 78
Cdd:PHA02874 172 IIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPL------------HNAIihNRSAIE 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214  79 IeaarkeeerimlrdarqWLNSGHINDvrHAKSGGTALHVAAAKGYT-EVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGK 157
Cdd:PHA02874 240 L-----------------LINNASIND--QDIDGSTPLHHAINPPCDiDIIDILLYHKADISIKDNKGENPIDTAFKYIN 300

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 219842214 158 EEAcrILVDNLCDMEMVNKVGQtafdVADEDILGYLEELQKKQ 200
Cdd:PHA02874 301 KDP--VIKDIIANAVLIKEADK----LKDSDFLEHIEIKDNKE 337
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 16-222 1.71e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 48.71  E-value: 1.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214  16 DNEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLdiaeeeameellqnevnrqGVDIEAARKEEERIMLRDAR 95
Cdd:PLN03192 555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTAL-------------------WNAISAKHHKIFRILYHFAS 615

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214  96 qwLNSGHIndvrhaksGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMEMVN 175
Cdd:PLN03192 616 --ISDPHA--------AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 219842214 176 kvgqtafdvADEDILGY-LEELQKKQNLLHSEKRDKKSPLIESTANMD 222
Cdd:PLN03192 686 ---------TDDDFSPTeLRELLQKRELGHSITIVDSVPADEPDLGRD 724
PHA03095 PHA03095
ankyrin-like protein; Provisional
 85-193 3.16e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.71  E-value: 3.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214  85 EEERIMLRDARQWLNSGhiNDVRHAKS-GGTALHVAAAKG---YTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEA 160
Cdd:PHA03095  21 NASNVTVEEVRRLLAAG--ADVNFRGEyGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLD 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 219842214 161 C-RILVDNLCDMEMVNKVGQTAFDV------ADEDILGYL 193
Cdd:PHA03095  99 ViKLLIKAGADVNAKDKVGRTPLHVylsgfnINPKVIRLL 138
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 1-181 5.50e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.52  E-value: 5.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214   1 MVKFLVENGA--NINQPDNEGwiPLHAAASCGYLDIAEFLIGQGAHVGAV-NSEGDTPLDIAEEEameellqnevnrQGV 77
Cdd:PHA02875  50 AIKLLMKHGAipDVKYPDIES--ELHDAVEEGDVKAVEELLDLGKFADDVfYKDGMTPLHLATIL------------KKL 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214  78 DIeaarkeeerimlrdARQWLNSGHINDVRHAKSGgTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGK 157
Cdd:PHA02875 116 DI--------------MKLLIARGADPDIPNTDKF-SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD 180

                        170       180
                 ....*....|....*....|....
gi 219842214 158 EEACRILVDNLCDMEMVNKVGQTA 181
Cdd:PHA02875 181 IAICKMLLDSGANIDYFGKNGCVA 204
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 99-188 5.87e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.17  E-value: 5.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214  99 NSGHINDVRHAK--------SGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILV----- 165
Cdd:PLN03192 537 NAALLEELLKAKldpdigdsKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYhfasi 616

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 219842214 166 -------DNLC------DMEMVNKVGQTAFDVADED 188
Cdd:PLN03192 617 sdphaagDLLCtaakrnDLTAMKELLKQGLNVDSED 652
PHA02798 PHA02798
ankyrin-like protein; Provisional
 1-150 6.62e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 46.37  E-value: 6.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214   1 MVKFLVENGANINQPDNEGWIPLHAAASC-----GYLDIAEFLIGQGAHVGAVNSEGDTPLDIAEEEAMEELLQNEVN-- 73
Cdd:PHA02798  53 IVKLFINLGANVNGLDNEYSTPLCTILSNikdykHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFmi 132

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 219842214  74 RQGVDIEAARKEEERIMlrdaRQWLNSGHINDVrhaksggtalhvaaakgytEVLKLLIQAGYDVN-IKDYDGWTPLH 150
Cdd:PHA02798 133 ENGADTTLLDKDGFTML----QVYLQSNHHIDI-------------------EIIKLLLEKGVDINtHNNKEKYDTLH 187
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1-201 7.60e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.60  E-value: 7.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214   1 MVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDIAEEEAMEELLQNEV-NRQGVD- 78
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIdNRSNINk 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214  79 -----IEAARKE--EERIMLRDARQWLNSghINDVRHaksggTALHVAA-AKGYTEVLKLLIQAGYDVNIKDYDGWTPLH 150
Cdd:PHA02876 240 ndlslLKAIRNEdlETSLLLYDAGFSVNS--IDDCKN-----TPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLY 312

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 219842214 151 AAAHWGKE-EACRILVDNLCDMEMVNKVGQTAFDVA-----DEDILGYLEELQKKQN 201
Cdd:PHA02876 313 LMAKNGYDtENIRTLIMLGADVNAADRLYITPLHQAstldrNKDIVITLLELGANVN 369
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 114-140 1.08e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.88  E-value: 1.08e-04
                           10        20
                   ....*....|....*....|....*..
gi 219842214   114 TALHVAAAKGYTEVLKLLIQAGYDVNI 140
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 18-49 4.04e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.42  E-value: 4.04e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 219842214   18 EGWIPLHAAA-SCGYLDIAEFLIGQGAHVGAVN 49
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02798 PHA02798
ankyrin-like protein; Provisional
 1-180 4.36e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.06  E-value: 4.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214   1 MVKFLVENGANINQPDNEGWIPLHAAASCGYLDIAE---FLIGQGAHVGAVNSEGDTPLDIaeEEAMEELLQNEVNR--- 74
Cdd:PHA02798  91 IVKILIENGADINKKNSDGETPLYCLLSNGYINNLEillFMIENGADTTLLDKDGFTMLQV--YLQSNHHIDIEIIKlll 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214  75 -QGVDIEAARKEE-------------ERIMLRDARQWLNSGHI---NDVRHAKSGGTALH--VAAAKGYTEVLKLLIQAG 135
Cdd:PHA02798 169 eKGVDINTHNNKEkydtlhcyfkyniDRIDADILKLFVDNGFIinkENKSHKKKFMEYLNslLYDNKRFKKNILDFIFSY 248

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 219842214 136 YDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMEMVNKVGQT 180
Cdd:PHA02798 249 IDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNT 293
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 2-58 4.69e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.12  E-value: 4.69e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 219842214   2 VKFLVENGANINQPDNEGWIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDI 58
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLEL 154
Ank_4 pfam13637
Ankyrin repeats (many copies);
22-58 5.66e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 5.66e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 219842214   22 PLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDI 58
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHF 40
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 144-176 6.41e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.04  E-value: 6.41e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 219842214  144 DGWTPLHAAA-HWGKEEACRILVDNLCDMEMVNK 176
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 112-140 1.04e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 1.04e-03
                          10        20
                  ....*....|....*....|....*....
gi 219842214  112 GGTALHVAAAKGYTEVLKLLIQAGYDVNI 140
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 119-181 1.39e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.55  E-value: 1.39e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 219842214 119 AAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMEMVNKVGQTA 181
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTA 594
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1-192 1.71e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 42.17  E-value: 1.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214   1 MVKFLVENGANINQPDNEGWIPLHAAASC-GYLDIAEFL--------------IGQGAHVGAVNSEGDTPLDIAEeeame 65
Cdd:PHA02878  52 VVKSLLTRGHNVNQPDHRDLTPLHIICKEpNKLGMKEMIrsinkcsvfytlvaIKDAFNNRNVEIFKIILTNRYK----- 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214  66 ellqnevNRQGVDIEAARK--EEERIMLRDARQWLNSGHINDVRHAKSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDY 143
Cdd:PHA02878 127 -------NIQTIDLVYIDKksKDDIIEAEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 219842214 144 DGWTPLHAAAHWGKEEACRILVDNLCDMEMVNKVGQTAFDVADEDILGY 192
Cdd:PHA02878 200 TNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDY 248
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 102-185 1.85e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.90  E-value: 1.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214 102 HINDVRHaKSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRILVDNLCDMEMVNKVGQTA 181
Cdd:PHA02875  93 FADDVFY-KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTP 171


                 ....
gi 219842214 182 FDVA 185
Cdd:PHA02875 172 LIIA 175
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 780-943 2.53e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 2.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214 780 QEQQSDTEEGSNKKETQTDSISRYETSSTSAGDRYDSLLGRSGSYSYLEERKPY-SSRLEKDDSTDFKK---LYEQILAE 855
Cdd:COG4942   68 ARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPlALLLSPEDFLDAVRrlqYLKYLAPA 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214 856 NEKLKAQLHDTNMELTDLKLQLEKATQRQERF-----ADRSLLEMEKRERRALERRI-SEMEEELKMLPDLKADNQRLKD 929
Cdd:COG4942  148 RREQAEELRADLAELAALRAELEAERAELEALlaeleEERAALEALKAERQKLLARLeKELAELAAELAELQQEAEELEA 227

                        170
                 ....*....|....
gi 219842214 930 ENGALIRVISKLSK 943
Cdd:COG4942  228 LIARLEAEAAAAAE 241
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 2-185 5.18e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.43  E-value: 5.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214   2 VKFLVENGANINQPDnegwIPLHAAASCGYLDIAEFLIGQGAHVGAVNSEGDTPLDIAEEEAMEELLQNEVNRQGVDIEA 81
Cdd:PHA02876 227 IKAIIDNRSNINKND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNA 302

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219842214  82 ARKEEERIMLRDARQWLNSGHIN-------DVRHAKS-GGTALHVAAA-KGYTEVLKLLIQAGYDVNIKDYDGWTPLHAA 152
Cdd:PHA02876 303 KNIKGETPLYLMAKNGYDTENIRtlimlgaDVNAADRlYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYA 382

                        170       180       190
                 ....*....|....*....|....*....|...
gi 219842214 153 AHWGKEEACRILVDNLCDMEMVNKVGQTAFDVA 185
Cdd:PHA02876 383 AVRNNVVIINTLLDYGADIEALSQKIGTALHFA 415
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 94-164 5.48e-03

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.65  E-value: 5.48e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 219842214  94 ARQWLNSGHINDVRHAkSGGTALHVAAAKGYTEVLKLLIQAGYDVNIKDYDGWTPLHAAAHWGKEEACRIL 164
Cdd:PTZ00322  98 ARILLTGGADPNCRDY-DGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 144-173 7.53e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.87  E-value: 7.53e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 219842214   144 DGWTPLHAAAHWGKEEACRILVDNLCDMEM 173
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Jnk-SapK_ap_N pfam09744
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ...
 850-917 8.46e-03

JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.


Pssm-ID: 462875 [Multi-domain]  Cd Length: 150  Bit Score: 37.98  E-value: 8.46e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 219842214  850 EQILAENEKLKAQLHDTNMELTDLKLQLEKATQrQERFADRSLLEME---KRERRALERRISEMEEELKML 917
Cdd:pfam09744  39 ESLASRNQEHNVELEELREDNEQLETQYEREKA-LRKRAEEELEEIEdqwEQETKDLLSQVESLEEENRRL 108
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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